What The Lab Is Doing

During a typical year, the CBB laboratory collaborates with more than 60 industrial companies and institutions. Weekly meetings usually schedule work for 15 active projects. Although more than 90% of the CBB laboratory’s contract income is from the private sector, CBB services federal agencies and institutions. For example, collaborations have produced vaccines, antibiotics, anticancer drugs, polymers, BL2-LS pathogens (used to develop diagnostics and vaccines), biochemicals, enzymes, pharmaceutical intermediates, and derivatives of bioactive compounds.

Projects conducted at the CBB laboratories include:

Glycolate Oxidase (GO), a Platform Technology (Click for more details)

E. I. DuPont donated patents related to glycolate oxidase (GO) technology to The University of Iowa. CBB developed the process to produce high-cell-density fermentations of Pichia pastoris yielding large quantities of biocatalyst. CBB has installed all the safety measures to handle solvent additions with oxygen sparging during fermentation.

  • GO based production of pyruvate
  • GO based production of >98% (R)-Hydroxy Butyric Acid

For more information about (GO) technology, see the Glycolate Oxidase, a Platform Technology page.

See the contact information page for inquiries or for a sample of pyruvate or (R)-Hydroxyl Butyric Acid produced with (GO) technology,.

Caffeine Metabolism and Diagnostics

Caffeine (1,3,7-trimethylxanthine) is readily found in many plant species. It is also a common human dietary ingredient. An enzyme, caffeine dehydrogenase (Cdh), has been isolated from Pseudomonas sp. Strain CBB1 that catalyzes the reaction shown in Figure 1. Cdh has been characterized as a novel quino-protein that is highly specific for caffeine (Yu, et.al., 2008). The enzyme is highly suitable for developing a diagnostic test for caffeine, using NBT as the indicator dye, which turns dark blue in the presence of caffeine. A sample test with caffeine added to milk is shown in Figure 2. Cdh gene has been completely sequenced and functional cloning of the gene is in progress. This technology is available for licensing for various applications. Please see the contact information.

Several other caffeine degrading Pseudomonas have been isolated from soil that carry out N-demethylation of caffeine as shown in the Figure 3. These enzymes are suitable for production of alkylxanthines.

Ryan Summers, a PhD student in Dr. Subramanian's laboratory, presented a paper at the ASM 2011 Annual Meeting. His paper was selected by the ASM Communications Committee to be highlighted in the press room during the conference. This resulted in more than 60 citations on popular press with respect to “bacterial addiction to caffeine”.
“Purification, Cloning, and Functional Expression of NdmA and NdmB, Two Positional-Specific Methylxanthine N-Demethylases from Pseudomonas Putida CBB5”.

Figure 1 

 Figure 2

 Figure 3